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Information on EC 2.3.1.B43 - protein-lysine desuccinylase (NAD+)
for references in articles please use BRENDA:EC2.3.1.B43preliminary BRENDA-supplied EC number
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2.3.1.B43 protein-lysine desuccinylase (NAD+)Specify your search results
Word Map
- 2.3.1.B43
- superoxide
- sirtuins
- sirt1
- cytokine
- triphosphate
- flavin
-
ischemia
-
histochemical
-
phagocyte
-
oxidases
-
histochemistry
- apocynin
- angiotensin
- p47phox
- mononucleotide
-
neuroprotective
- nampt
-
phosphoribosyltransferase
- diaphorase
-
nicotinic
- nadph-diaphorase
- nadph-d
-
nad-dependent
- adp-ribose
- glucose-6-phosphate
- parps
-
polyadp-ribose
-
deacetylases
-
granulomatous
-
deacetylation
- gp91phox
-
autofluorescence
-
adp-ribosylation
- nadph-oxidase
-
iodonium
-
ii-induced
- nnos
-
phosphate-dependent
-
riboside
- diphenyleneiodonium
-
adenylyltransferase
-
oxidase-dependent
-
adp-ribosyltransferases
-
polymerase-1
-
electrocatalytic
-
nitrergic
-
diphenylene
-
oxidase-derived
- polyadenosine
-
g6pd-deficient
- medicine
The expected taxonomic range for this enzyme is: Archaea, Bacteria, Eukaryota
Reaction Schemes
Synonyms
CobB, CobB Sir2 protein, NAD+-dependent protein deacetylase, NAD+-dependent sirtuin deacetylase, nicotinamide adenine dinucleotide, nicotinamide adenine dinucleotide-dependent protein deacetylase, Sir2Af1, SIRT5, SIRT5iso1, SIRT5iso2, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CobB
NAD+-dependent protein deacetylase
nicotinamide adenine dinucleotide-dependent protein deacetylase
SIRT5
SIRT5iso1
SIRT5 isoforms (i.e., SIRT5iso1 and SIRT5iso2) are encoded by the human SIRT5 gene. Their C-termini slightly differ from each other. Although both isoforms contain cleavable mitochondrial targeting signals at their N-termini, it is found that the cleaved SIRT5iso2 is localized mainly in mitochondria, whereas the cleaved SIRT5iso1 is localized in both mitochondria and cytoplasm
SIRT5iso2
SIRT5 isoforms (i.e., SIRT5iso1 and SIRT5iso2) are encoded by the human SIRT5 gene. Their C-termini slightly differ from each other. Although both isoforms contain cleavable mitochondrial targeting signals at their N-termini, it is found that the cleaved SIRT5iso2 is localized mainly in mitochondria, whereas the cleaved SIRT5iso1 is localized in both mitochondria and cytoplasm. SIRT5iso2 is a primate-specific isoform
sirtuin 5
SIRT5
-
SIRT5
SIRT5 isoforms (i.e., SIRT5iso1 and SIRT5iso2) are encoded by the human SIRT5 gene. Their C-termini slightly differ from each other. Although both isoforms contain cleavable mitochondrial targeting signals at their N-termini, it is found that the cleaved SIRT5iso2 is localized mainly in mitochondria, whereas the cleaved SIRT5iso1 is localized in both mitochondria and cytoplasm
sirtuin 5
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
NAD+ + [protein]-N6-acetyl-L-lysine = nicotinamide + [protein]-L-lysine + 2'-O-acetyl-ADP-ribose
NAD+ + [protein]-N6-succinyl-L-lysine = nicotinamide + [protein]-L-lysine + 2'-O-succinyl-ADP-ribose
NAD+ + [protein]-N6-acetyl-L-lysine = nicotinamide + [protein]-L-lysine + 2'-O-acetyl-ADP-ribose
crystallographic evidence is provided that 2'-O-acetyl ADP-ribose is a final product in the Sir2 reaction. A revised mechanism for catalysis based on the structural and functional characterization of Sir2 mutants is proposed. In this mechanism, the activation of the 2'-OH of nicotinamide ribose by His-116 is essential for the hydrolysis of the acetyl groups from N-acetyl lysine. The conserved Ser-24 and Asp-101 participate in the stabilization of local structure for NAD binding rather than direct involvement in catalysis
-
NAD+ + [protein]-N6-acetyl-L-lysine = nicotinamide + [protein]-L-lysine + 2'-O-acetyl-ADP-ribose
-
-
-
-
NAD+ + [protein]-N6-succinyl-L-lysine = nicotinamide + [protein]-L-lysine + 2'-O-succinyl-ADP-ribose
most efficient at catalyzing desuccinylation, medium-chain deacylation (octanoyl-, decanoyl-, dodecanoyl-) is catalyzed with lower activity
-
NAD+ + [protein]-N6-succinyl-L-lysine = nicotinamide + [protein]-L-lysine + 2'-O-succinyl-ADP-ribose
-
-
-
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
NAD+ + Ac-(N6-methylmalonyl)Lys-(7-amido-4-methylcoumarin)
nicotinamide + Ac-Lys-7-amido-4-methylcoumarin + 2'-O-methylmalonyl-ADP-ribose
-
-
-
-
?
NAD+ + Ac-(N6-succinyl)Lys-7-amido-4-methylcoumarin
nicotinamide + Ac-Lys-7-amido-4-methylcoumarin + 2'-O-succinyl-ADP-ribose
-
-
-
-
?
NAD+ + Ac-Leu-Gly-(N6-malonyl)Lys-7-amido-4-methylcoumarin
nicotinamide + Ac-Leu-Gly-Lys-7-amido-4-methylcoumarin + 2'-O-malonyl-ADP-ribose
-
-
-
-
?
NAD+ + Ac-Leu-Gly-(N6-succinyl)Lys-7-amido-4-methylcoumarin
nicotinamide + Ac-Leu-Gly-Lys-7-amido-4-methylcoumarin + 2'-O-succinyl-ADP-ribose
-
-
-
-
?
NAD+ + AFNQG(N6-malonyl)KIFK
nicotinamide + AFNQGKIFK + 2'-O-malonyl-ADP-ribose
-
-
-
-
?
NAD+ + AYVDDTPAEQM(N6-malonyl)KAER
nicotinamide + AYVDDTPAEQMKAER + 2'-O-malonyl-ADP-ribose
-
-
-
-
?
NAD+ + benzoyl-GVL(N6-acetyl)KEYGV-amide
nicotinamide + benzoyl-GVLKEYGV-amide + 2'-O-acetyl-ADP-ribose
-
-
-
-
?
NAD+ + benzoyl-GVL(N6-adipoyl)KEYGV-amide
nicotinamide + benzoyl-GVLKEYGV-amide + 2'-O-adipoyl-ADP-ribose
-
-
-
-
?
NAD+ + benzoyl-GVL(N6-glutaryl)KEYGV-amide
nicotinamide + benzoyl-GVLKEYGV-amide + 2'-O-glutaryl-ADP-ribose
-
-
-
-
?
NAD+ + benzoyl-GVL(N6-malonyl)KEYGV-amide
nicotinamide + benzoyl-GVLKEYGV-amide + 2'-O-malonyl-ADP-ribose
-
-
-
-
?
NAD+ + benzoyl-GVL(N6-oxalyl)KEYGV-amide
nicotinamide + benzoyl-GVLKEYGV-amide + 2'-O-oxalyl-ADP-ribose
-
-
-
-
?
NAD+ + benzoyl-GVL(N6-pimeloyl)KEYGV-amide
nicotinamide + benzoyl-GVLKEYGV-amide + 2'-O-pimeloyl-ADP-ribose
-
-
-
-
?
NAD+ + benzoyl-GVL(N6-suberoyl)KEYGV-amide
nicotinamide + benzoyl-GVLKEYGV-amide + 2'-O-suberoyl-ADP-ribose
-
-
-
-
?
NAD+ + benzoyl-GVL(N6-succinyl)KEYGV-amide
nicotinamide + benzoyl-GVLKEYGV-amide + 2'-O-succinyl-ADP-ribose
-
-
-
-
?
NAD+ + benzoyl-RGVL(N6-succinyl)KEYGV-amide
nicotinamide + benzoyl-RGVLKEYGV-amide + 2'-O-acetyl-ADP-ribose
-
carbamoyl phosphate synthetase 1 Lys527 peptide
-
-
?
NAD+ + DSYVGDEAQSDSYVGDEAQS(N6-malonyl)KR
nicotinamide + DSYVGDEAQSDSYVGDEAQSKR + 2'-O-malonyl-ADP-ribose
-
-
-
-
?
NAD+ + ETGVDLT(N6-succinyl)KDNMALQR
nicotinamide + ETGVDLTKDNMALQR + 2'-O-succinyl-ADP-ribose
-
-
-
-
?
NAD+ + IEEELGS(N6-malonyl)KAK
nicotinamide + IEEELGSKAK + 2'-O-malonyl-ADP-ribose
-
-
-
-
?
NAD+ + KGLGKGGA(N6-propionyl)KRHRKW
nicotinamide + KGLGKGGAKRHRKW + 2'-O-propionyl-ADP-ribose
NAD+ + KGLGKGGA(N6-succinyl)KRHRKW
nicotinamide + KGLGKGGAKRHRKW + 2'-O-succinyl-ADP-ribose
NAD+ + KQTAR(N6-malonyl)KSTGGWW
nicotinamide + KQTARKSTGGWW + 2'-O-malonyl-ADP-ribose
-
histone H3K9 malonyl peptide
-
-
?
NAD+ + KQTAR(N6-succinyl)KSTGGKA
nicotinamide + KQTARKSTGGKA + 2'-O-succinyl-ADP-ribose
-
-
-
-
?
NAD+ + KQTAR(N6-succinyl)KSTGGWW
nicotinamide + KQTARKSTGGWW + 2'-O-succinyl-ADP-ribose
-
histone H3K9 succinyl peptide
-
-
?
NAD+ + KTRSG(N6-malonyl)KVMRRWW
nicotinamide + KTRSGKVMRRWW + 2'-O-malonyl-ADP-ribose
-
-
-
-
?
NAD+ + KTRSG(N6-succinyl)KVMRRWW
nicotinamide + KTRSGKVMRRWW + 2'-O-succinyl-ADP-ribose
-
ACS2 Lys628 peptide
-
-
?
NAD+ + N2-benzyloxycarbonyl-N6-succinyl-L-lysine-7-amido-4-methylcoumarin
nicotinamide + N2-benzyloxycarbonyl-L-lysine-7-amido-4-methylcoumarin + 2'-O-succinyl-ADP-ribose
i.e. 3-[(5-[[(benzyloxy)carbonyl]amino]-5-[(4-methyl-2-oxo-2H-chromen-7-yl)carbamoyl]pentyl)carbamoyl]-propanoic acid
-
-
?
NAD+ + QTAR(N6-acetyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-acetyl-ADP-ribose
-
acetylated histone H3 peptide, less than 10% compared to the activity with the succinylated peptide
-
-
?
NAD+ + QTAR(N6-decanoyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-decanoyl-ADP-ribose
-
decanoylated histone H3 peptide, about 35% compared to the activity with the succinylated peptide
-
-
?
NAD+ + QTAR(N6-dodecanoyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-dodecanoyl-ADP-ribose
-
dodecanoylated histone H3 peptide, about 35% compared to the activity with the succinylated peptide
-
-
?
NAD+ + QTAR(N6-hexanoyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-hexanoyl-ADP-ribose
-
hexanoylated histone H3 peptide, less than 10% compared to the activity with the succinylated peptide
-
-
?
NAD+ + QTAR(N6-myristoyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-myristoyl-ADP-ribose
-
myristoylated histone H3 peptide, about 15% compared to the activity with the succinylated peptide
-
-
?
NAD+ + QTAR(N6-octanoyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-octanoyl-ADP-ribose
-
octanoylated histone H3 peptide, about 30% compared to the activity with the succinylated peptide
-
-
?
NAD+ + QTAR(N6-propionyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-propionyl-ADP-ribose
-
propionylated histone H3 peptide, less than 10% compared to the activity with the succinylated peptide
-
-
?
NAD+ + QTAR(N6-succinyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-succinyl-ADP-ribose
-
succinylated histone H3 peptide
-
-
?
NAD+ + SGASE(N6-malonyl)KDIVHSGWW
nicotinamide + SGASEKDIVHSGWW + 2'-O-malonyl-ADP-ribose
-
-
-
-
?
NAD+ + SGASE(N6-succinyl)KDIVHSGWW
nicotinamide + SGASEKDIVHSGWW + 2'-O-succinyl-ADP-ribose
-
glutamate dehydrogenase Lys503 peptide
-
-
?
NAD+ + SKEYFS(N6-succinyl)KQK
nicotinamide + SKEYFSKQK + 2'-O-acetyl-ADP-ribose
-
-
-
-
?
NAD+ + SQG(N6-succinyl)KVLQATVV
nicotinamide + SQGKVLQATVV + 2'-O-succinyl-ADP-ribose
-
-
-
-
?
NAD+ + TAIG(N6-malonyl)KAGYTDK
nicotinamide + TAIGKAGYTDK + 2'-O-malonyl-ADP-ribose
-
-
-
-
?
NAD+ + TRSG(N6-acetyl)KVMR
nicotinamide + TRSGKVMR + 2'-O-acetyl-ADP-ribose
-
peptide based on an acetyl-CoA synthetase 2 acetylation site
-
-
?
NAD+ + VLLPEYGGT(N6-succinyl)KVVLDDK
nicotinamide + VLLPEYGGTKVVLDDK + 2'-O-succinyl-ADP-ribose
-
-
-
-
?
NAD+ + [acetyl-coenzyme A synthetase]-N6-acetyl-L-lysine609
nicotinamide + [acetyl-coenzyme A synthetase]-L-lysine609 + 2'-O-acetyl-ADP-ribose
NAD+ + [bovine serum albumin]-N6-acetyl-L-lysine
nicotinamide + [bovine serum albumin]-L-lysine + 2'-O-acetyl-ADP-ribose
crystallographic evidence is provided that 2'-O-acetyl ADP-ribose is a final product in the Sir2 reaction. A revised mechanism for catalysis based on the structural and functional characterization of Sir2 mutants is proposed. In this mechanism, the activation of the 2'-OH of nicotinamide ribose by His-116 is essential for the hydrolysis of the acetyl groups from N-acetyl lysine. The conserved Ser-24 and Asp-101 participate in the stabilization of local structure for NAD binding rather than direct involvement in catalysis
-
-
?
NAD+ + [carbamoyl phosphate synthase 1]-N6-acetyl-L-lysine
nicotinamide + [carbamoyl phosphate synthase 1]-L-lysine + 2'-O-acetyl-ADP ribose
NAD+ + [carbamoyl phosphate synthase 1]-N6-acetyl-L-lysine
nicotinamide + [carbamoyl phosphate synthase 1]-L-lysine + 2'-O-acetyl-ADP-ribose
NAD+ + [carbamoyl phosphate synthase 1]-N6-succinyl-L-lysine
nicotinamide + [carbamoyl phosphate synthase 1]-L-lysine + 2'-O-succinyl-ADP ribose
-
deletion of Sirt5 in mice increases the level of succinylation on carbamoyl phosphate synthase 1
-
-
?
NAD+ + [carbamoyl phosphate synthetase 1 derived glutarylated peptide]-N6-acetyl-L-lysine
nicotinamide + [carbamoyl phosphate synthetase 1 derived glutarylated peptide]-L-lysine + 2'-O-acetyl-ADP-ribose
-
-
-
-
?
NAD+ + [carbamoyl phosphate synthetase 1]-N6-acetyl-L-lysine
nicotinamide + [carbamoyl phosphate synthetase 1]-L-lysine + 2'-O-acetyl-ADP ribose
NAD+ + [carbamoyl phosphate synthetase 1]-N6-glutaryl-L-lysine
nicotinamide + [carbamoyl phosphate synthetase 1]-L-lysine + 2'-O-glutaryl-ADP-ribose
-
-
-
-
?
NAD+ + [chicken histone]-N6-acetyl-L-lysine
nicotinamide + [chicken histone]-L-lysine + 2'-O-acetyl-ADP-ribose
-
chemically acetylated chicken histone. Less activity toward chemically acetylated bovine serum albumin and monoacetylated histone H4 (K16 and K8). No activity is observed with monoacetylated histone K5 and K12 histone H4 peptides
-
-
?
NAD+ + [Cu/Zn superoxide dismutase]-N6-succinyl-L-lysine123
nicotinamide + [Cu/Zn superoxide dismutase]-L-lysine123 + 2'-O-succinyl-ADP-ribose
NAD+ + [cytochrome c]-N6-acetyl-L-lysine
nicotinamide + [cytochrome c]-L-lysine + 2'-O-acetyl-ADP-ribose
-
-
-
-
?
NAD+ + [forkhead box O3]-N6-acetyl-L-lysine
nicotinamide + [forkhead box O3]-L-lysine + 2'-O-acetyl-ADP-ribose
-
the enzyme deacetylates FOXO3 at K271 and K290
-
-
?
NAD+ + [glucose-6-phosphate dehydrogenase]-N6-acetyl-L-lysine
nicotinamide + [glucose-6-phosphate dehydrogenase]-L-lysine + 2'-O-acetyl-ADP-ribose
-
-
-
-
?
NAD+ + [glyceraldehyde-3-phosphate dehydrogenase]-N6-malonyl-L-lysine
nicotinamide + [glyceraldehyde-3-phosphate dehydrogenase]-L-lysine + 2'-O-malonyl-ADP-ribose
-
-
-
-
?
NAD+ + [histone H3 K9 peptide]-N6-acetyl-L-lysine
nicotinamide + [histone H3 K9 peptide]-L-lysine + 2'-O-acetyl-ADP-ribose
-
-
-
-
?
NAD+ + [histone H3 K9 peptide]-N6-succinyl-L-lysine
nicotinamide + [histone H3 K9 peptide]-L-lysine + 2'-O-succinyl-ADP-ribose
-
-
-
-
?
NAD+ + [isocitrate dehydrogenase 2]-N6-acetyl-L-lysine
nicotinamide + [isocitrate dehydrogenase 2]-L-lysine + 2'-O-acetyl-ADP-ribose
-
-
-
-
?
NAD+ + [N-hydroxyarylamine O-acetyltransferase]-N6-acetyl-L-lysine
nicotinamide + [N-hydroxyarylamine O-acetyltransferase]-L-lysine + 2'-O-acetyl-ADP-ribose
NAD+ + [peptide derived from carbamoyl phosphate synthetase 1]-N6-acetyl-L-lysine
nicotinamide + [peptide derived from carbamoyl phosphate synthetase 1]-L-lysine + 2'-O-acetyl-ADP-ribose
-
-
-
-
?
NAD+ + [protein]-N6-acetyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-acetyl-ADP-ribose
NAD+ + [protein]-N6-malonyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-malonyl-ADP-ribose
NAD+ + [protein]-N6-succinyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-succinyl-ADP-ribose
NAD+ + [PrpE protein]-N6-acetyl-L-lysine
nicotinamide + [PrpE protein]-L-lysine + 2'-O-acetyl-ADP ribose
-
-
-
-
?
NAD+ + [PrpE protein]-N6-propionyl-L-lysine
nicotinamide + [PrpE protein]-L-lysine + 2'-O-propionyl-ADP-ribose
NAD+ + [pyruvate dehydrogenase complex]-N6-succinyl-L-lysine
nicotinamide + [pyruvate dehydrogenase complex]-L-lysine + O-succinyl-ADP-ribose
NAD+ + [RcsB protein]-N6-acetyl-L-lysine180
nicotinamide + [RcsB protein]-L-lysine180 + 2'-O-acetyl-ADP-ribose
NAD+ + [response regulator CheY]-N6-acetyl-L-lysine
nicotinamide + [response regulator CheY]-L-lysine + 2'-O-acetyl-ADP-ribose
NAD+ + [succinate dehydrogenase]-N6-succinyl-L-lysine
nicotinamide + [succinate dehydrogenase]-L-lysine + O-succinyl-ADP-ribose
NAD+ + [urate oxidase]-N6-acetyl-L-lysine
nicotinamide + [urate oxidase]-L-lysine + 2'-O-acetyl-ADP-ribose
NAD+ + FKRGVL(N6-acetyl)KEYGVKV
nicotinamide + FKRGVLKEYGVKV + 2'-O-acetyl-ADP-ribose
-
acetylated peptide derived from carbamoylphosphate synthetase 1 (CPS1)
-
-
?
NAD+ + FKRGVL(N6-acetyl)KEYGVKV
nicotinamide + FKRGVLKEYGVKV + 2'-O-acetyl-ADP-ribose
-
carbamoyl phosphate synthetase 1 Lys527 peptide
-
-
?
NAD+ + KGLGKGGA(N6-acetyl)KRHRKW
nicotinamide + KGLGKGGAKRHRKW + 2'-O-acetyl-ADP-ribose
-
the rate of desuccinylation is about 5fold faster than the rate of deacetylation
-
-
?
NAD+ + KGLGKGGA(N6-acetyl)KRHRKW
nicotinamide + KGLGKGGAKRHRKW + 2'-O-acetyl-ADP-ribose
-
the rate of desuccinylation is 2.3fold faster than the rate of deacetylation
-
-
?
NAD+ + KGLGKGGA(N6-butyryl)KRHRKW
nicotinamide + KGLGKGGAKRHRKW + 2'-O-butyryl-ADP-ribose
-
the rate of desuccinylation is about 10fold faster than the rate of debutyrylation
-
-
?
NAD+ + KGLGKGGA(N6-butyryl)KRHRKW
nicotinamide + KGLGKGGAKRHRKW + 2'-O-butyryl-ADP-ribose
-
the rate of desuccinylation is 5.8fold faster than the rate of deburyrylation
-
-
?
NAD+ + KGLGKGGA(N6-propionyl)KRHRKW
nicotinamide + KGLGKGGAKRHRKW + 2'-O-propionyl-ADP-ribose
-
the rate of desuccinylation is about 5fold faster than the rate of depropionylation
-
-
?
NAD+ + KGLGKGGA(N6-propionyl)KRHRKW
nicotinamide + KGLGKGGAKRHRKW + 2'-O-propionyl-ADP-ribose
-
the rate of desuccinylation is 3.8fold faster than the rate of depropionylation
-
-
?
NAD+ + KGLGKGGA(N6-succinyl)KRHRKW
nicotinamide + KGLGKGGAKRHRKW + 2'-O-succinyl-ADP-ribose
-
the rate of desuccinylation is about 5fold faster than the rate of deacetylation
-
-
?
NAD+ + KGLGKGGA(N6-succinyl)KRHRKW
nicotinamide + KGLGKGGAKRHRKW + 2'-O-succinyl-ADP-ribose
-
the rate of desuccinylation is 2.3fold faster than the rate of deacetylation
-
-
?
NAD+ + [acetyl-coenzyme A synthetase]-N6-acetyl-L-lysine609
nicotinamide + [acetyl-coenzyme A synthetase]-L-lysine609 + 2'-O-acetyl-ADP-ribose
-
-
-
-
?
NAD+ + [acetyl-coenzyme A synthetase]-N6-acetyl-L-lysine609
nicotinamide + [acetyl-coenzyme A synthetase]-L-lysine609 + 2'-O-acetyl-ADP-ribose
-
deacetylation by CobB activates the acetyl-coenzyme A synthetase
-
-
?
NAD+ + [carbamoyl phosphate synthase 1]-N6-acetyl-L-lysine
nicotinamide + [carbamoyl phosphate synthase 1]-L-lysine + 2'-O-acetyl-ADP ribose
-
-
-
-
?
NAD+ + [carbamoyl phosphate synthase 1]-N6-acetyl-L-lysine
nicotinamide + [carbamoyl phosphate synthase 1]-L-lysine + 2'-O-acetyl-ADP ribose
-
SIRT5 deacetylates carbamoyl phosphate synthetase 1 (CPS1), an enzyme which is the first and rate-limiting step of urea cycle. Deacetylation of CPS1 by SIRT5 results in activation of CPS1 enzymatic activity
-
-
?
NAD+ + [carbamoyl phosphate synthase 1]-N6-acetyl-L-lysine
nicotinamide + [carbamoyl phosphate synthase 1]-L-lysine + 2'-O-acetyl-ADP-ribose
-
-
-
?
NAD+ + [carbamoyl phosphate synthase 1]-N6-acetyl-L-lysine
nicotinamide + [carbamoyl phosphate synthase 1]-L-lysine + 2'-O-acetyl-ADP-ribose
SIRT5 deacetylates carbamoyl phosphate synthetase 1 (CPS1), an enzyme which is the first and rate-limiting step of urea cycle
-
-
?
NAD+ + [carbamoyl phosphate synthetase 1]-N6-acetyl-L-lysine
nicotinamide + [carbamoyl phosphate synthetase 1]-L-lysine + 2'-O-acetyl-ADP ribose
-
-
-
-
?
NAD+ + [carbamoyl phosphate synthetase 1]-N6-acetyl-L-lysine
nicotinamide + [carbamoyl phosphate synthetase 1]-L-lysine + 2'-O-acetyl-ADP ribose
-
SIRT5 plays a pivotal role in ammonia detoxification and disposal by activating carbamoyl phosphate synthetase 1 (CPS1) an enzyme, catalyzing the initial step of the urea cycle for ammonia detoxification and disposal. SIRT5 deacetylates CPS1 and up-regulates its activity. During fasting, NAD+ in liver mitochondria increases, thereby triggering SIRT5 deacetylation of CPS1 and adaptation to the increase in amino acid catabolism. Indeed, SIRT5 KO mice fail to up-regulate CPS1 activity and show elevated blood ammonia during fasting
-
-
?
NAD+ + [Cu/Zn superoxide dismutase]-N6-succinyl-L-lysine123
nicotinamide + [Cu/Zn superoxide dismutase]-L-lysine123 + 2'-O-succinyl-ADP-ribose
-
-
-
-
?
NAD+ + [Cu/Zn superoxide dismutase]-N6-succinyl-L-lysine123
nicotinamide + [Cu/Zn superoxide dismutase]-L-lysine123 + 2'-O-succinyl-ADP-ribose
-
SIRT5 binds to, desuccinylates and activates the key antioxidant enzyme Cu/Zn superoxide dismutase (SOD1). SOD1-mediated reduction of reactive oxygen species (ROS) is increased when SIRT5 is co-expressed. Posttranslational regulation of SOD1 by means of succinylation and SIRT5-dependent desuccinylation is important for the growth of lung tumor cells
-
-
?
NAD+ + [N-hydroxyarylamine O-acetyltransferase]-N6-acetyl-L-lysine
nicotinamide + [N-hydroxyarylamine O-acetyltransferase]-L-lysine + 2'-O-acetyl-ADP-ribose
-
-
-
-
?
NAD+ + [N-hydroxyarylamine O-acetyltransferase]-N6-acetyl-L-lysine
nicotinamide + [N-hydroxyarylamine O-acetyltransferase]-L-lysine + 2'-O-acetyl-ADP-ribose
-
-
-
-
?
NAD+ + [protein]-N6-acetyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-acetyl-ADP-ribose
-
the enzyme regulates protein function in diverse and often essential cellular processes, most notably translation
-
-
?
NAD+ + [protein]-N6-acetyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-acetyl-ADP-ribose
-
the enzyme can deacetylate acetyllysine independently whether the acetyl donor is acetyl-Coenzyme A or acetyl phosphate. Linear sequences alone are inadequate to predict CobB substrates and that structural analyses are necessary. CobB substrate acetyllyines appear to be located near the surface of the protein on a
-
-
?
NAD+ + [protein]-N6-acetyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-acetyl-ADP-ribose
-
weak deacetylase activity
-
-
?
NAD+ + [protein]-N6-malonyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-malonyl-ADP-ribose
-
-
-
-
?
NAD+ + [protein]-N6-malonyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-malonyl-ADP-ribose
-
-
-
-
?
NAD+ + [protein]-N6-succinyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-succinyl-ADP-ribose
-
-
-
-
?
NAD+ + [protein]-N6-succinyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-succinyl-ADP-ribose
-
protein lysine succinylation may represent a posttranslational modification that can be reversed by Sirt5 in vivo. Lysine succinylation occurs on several mammalian proteins
-
-
?
NAD+ + [protein]-N6-succinyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-succinyl-ADP-ribose
-
strong succinylase activity
-
-
?
NAD+ + [protein]-N6-succinyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-succinyl-ADP-ribose
-
-
-
-
?
NAD+ + [PrpE protein]-N6-propionyl-L-lysine
nicotinamide + [PrpE protein]-L-lysine + 2'-O-propionyl-ADP-ribose
-
-
-
-
?
NAD+ + [PrpE protein]-N6-propionyl-L-lysine
nicotinamide + [PrpE protein]-L-lysine + 2'-O-propionyl-ADP-ribose
-
N-Lysine propionylation controls the activity of propionyl-CoA synthetase
-
-
?
NAD+ + [pyruvate dehydrogenase complex]-N6-succinyl-L-lysine
nicotinamide + [pyruvate dehydrogenase complex]-L-lysine + O-succinyl-ADP-ribose
-
-
-
-
?
NAD+ + [pyruvate dehydrogenase complex]-N6-succinyl-L-lysine
nicotinamide + [pyruvate dehydrogenase complex]-L-lysine + O-succinyl-ADP-ribose
-
SIRT5 represses biochemical activity of, and cellular respiration through, the protein complex
-
-
?
NAD+ + [RcsB protein]-N6-acetyl-L-lysine180
nicotinamide + [RcsB protein]-L-lysine180 + 2'-O-acetyl-ADP-ribose
-
-
-
-
?
NAD+ + [RcsB protein]-N6-acetyl-L-lysine180
nicotinamide + [RcsB protein]-L-lysine180 + 2'-O-acetyl-ADP-ribose
-
acetylation of the response regulator RcsB controls transcription from the small RNA promoter rprA
-
-
?
NAD+ + [RcsB protein]-N6-acetyl-L-lysine180
nicotinamide + [RcsB protein]-L-lysine180 + 2'-O-acetyl-ADP-ribose
-
reversible Nepsilon-Lys acetylation of transcription factors is a mode of regulation of gene expression used by all cells
-
-
?
NAD+ + [response regulator CheY]-N6-acetyl-L-lysine
nicotinamide + [response regulator CheY]-L-lysine + 2'-O-acetyl-ADP-ribose
-
-
-
-
?
NAD+ + [response regulator CheY]-N6-acetyl-L-lysine
nicotinamide + [response regulator CheY]-L-lysine + 2'-O-acetyl-ADP-ribose
-
the enzyme regulates chemotaxis of Escherichia coli by deacetylating CheY
-
-
?
NAD+ + [response regulator CheY]-N6-acetyl-L-lysine
nicotinamide + [response regulator CheY]-L-lysine + 2'-O-acetyl-ADP-ribose
Escherichia coli W3110 / ATCC 27325
-
-
-
-
?
NAD+ + [response regulator CheY]-N6-acetyl-L-lysine
nicotinamide + [response regulator CheY]-L-lysine + 2'-O-acetyl-ADP-ribose
Escherichia coli W3110 / ATCC 27325
-
the enzyme regulates chemotaxis of Escherichia coli by deacetylating CheY
-
-
?
NAD+ + [succinate dehydrogenase]-N6-succinyl-L-lysine
nicotinamide + [succinate dehydrogenase]-L-lysine + O-succinyl-ADP-ribose
-
-
-
-
?
NAD+ + [succinate dehydrogenase]-N6-succinyl-L-lysine
nicotinamide + [succinate dehydrogenase]-L-lysine + O-succinyl-ADP-ribose
-
SIRT5 represses biochemical activity of, and cellular respiration through, the protein complex
-
-
?
NAD+ + [urate oxidase]-N6-acetyl-L-lysine
nicotinamide + [urate oxidase]-L-lysine + 2'-O-acetyl-ADP-ribose
-
-
-
-
?
NAD+ + [urate oxidase]-N6-acetyl-L-lysine
nicotinamide + [urate oxidase]-L-lysine + 2'-O-acetyl-ADP-ribose
-
SIRT5 activates urate oxidase through deacetylation in mouse liver mitochondria
-
-
?
additional information
?
-
-
it is proposed that YfiQ and CobB catalyze the reversible acetylation of a protein that mediates carbon-induced cpxP transcription
-
-
-
additional information
?
-
-
global identification of CobB substrates using an Escherichia coli proteome microarray
-
-
-
additional information
?
-
-
the enzyme shows dual enzymatic activities to catalyze the removal of two structurally different lysine acyl groups, acetyl and succinyl, from the modified lysine residues
-
-
-
additional information
?
-
-
global identification of CobB substrates using an Escherichia coli proteome microarray
-
-
-
additional information
?
-
-
catalytic efficiency (kcat/Km) of Sirt5 with the histone H3K9 acetyl peptide is about 500fold lower than that of Sirt1. Sirtuin 5 has only weak deacetylase activity. Difference in substrate specificity is probably due to a larger hydrophobic pocket with 2 residues (Tyr102 and Arg105) that bind to malonylated and succinylated substrates and define the specificity
-
-
-
additional information
?
-
-
no activity with Ac-Leu-Gly-(N6-acetyl)Lys-7-amido-4-methylcoumarin
-
-
-
additional information
?
-
-
Sirt5 does not deacetylate glutamate dehydrogenase or isocitrate dehydrogenase 2
-
-
-
additional information
?
-
-
Sirt5 shows negligible activity toward lysine deacetylation
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
NAD+ + [acetyl-coenzyme A synthetase]-N6-acetyl-L-lysine609
nicotinamide + [acetyl-coenzyme A synthetase]-L-lysine609 + 2'-O-acetyl-ADP-ribose
-
deacetylation by CobB activates the acetyl-coenzyme A synthetase
-
-
?
NAD+ + [carbamoyl phosphate synthase 1]-N6-acetyl-L-lysine
nicotinamide + [carbamoyl phosphate synthase 1]-L-lysine + 2'-O-acetyl-ADP ribose
-
SIRT5 deacetylates carbamoyl phosphate synthetase 1 (CPS1), an enzyme which is the first and rate-limiting step of urea cycle. Deacetylation of CPS1 by SIRT5 results in activation of CPS1 enzymatic activity
-
-
?
NAD+ + [carbamoyl phosphate synthase 1]-N6-acetyl-L-lysine
nicotinamide + [carbamoyl phosphate synthase 1]-L-lysine + 2'-O-acetyl-ADP-ribose
Q8K2C6
SIRT5 deacetylates carbamoyl phosphate synthetase 1 (CPS1), an enzyme which is the first and rate-limiting step of urea cycle
-
-
?
NAD+ + [carbamoyl phosphate synthase 1]-N6-succinyl-L-lysine
nicotinamide + [carbamoyl phosphate synthase 1]-L-lysine + 2'-O-succinyl-ADP ribose
-
deletion of Sirt5 in mice increases the level of succinylation on carbamoyl phosphate synthase 1
-
-
?
NAD+ + [carbamoyl phosphate synthetase 1]-N6-acetyl-L-lysine
nicotinamide + [carbamoyl phosphate synthetase 1]-L-lysine + 2'-O-acetyl-ADP ribose
-
SIRT5 plays a pivotal role in ammonia detoxification and disposal by activating carbamoyl phosphate synthetase 1 (CPS1) an enzyme, catalyzing the initial step of the urea cycle for ammonia detoxification and disposal. SIRT5 deacetylates CPS1 and up-regulates its activity. During fasting, NAD+ in liver mitochondria increases, thereby triggering SIRT5 deacetylation of CPS1 and adaptation to the increase in amino acid catabolism. Indeed, SIRT5 KO mice fail to up-regulate CPS1 activity and show elevated blood ammonia during fasting
-
-
?
NAD+ + [carbamoyl phosphate synthetase 1]-N6-glutaryl-L-lysine
nicotinamide + [carbamoyl phosphate synthetase 1]-L-lysine + 2'-O-glutaryl-ADP-ribose
-
-
-
-
?
NAD+ + [Cu/Zn superoxide dismutase]-N6-succinyl-L-lysine123
nicotinamide + [Cu/Zn superoxide dismutase]-L-lysine123 + 2'-O-succinyl-ADP-ribose
-
SIRT5 binds to, desuccinylates and activates the key antioxidant enzyme Cu/Zn superoxide dismutase (SOD1). SOD1-mediated reduction of reactive oxygen species (ROS) is increased when SIRT5 is co-expressed. Posttranslational regulation of SOD1 by means of succinylation and SIRT5-dependent desuccinylation is important for the growth of lung tumor cells
-
-
?
NAD+ + [forkhead box O3]-N6-acetyl-L-lysine
nicotinamide + [forkhead box O3]-L-lysine + 2'-O-acetyl-ADP-ribose
-
the enzyme deacetylates FOXO3 at K271 and K290
-
-
?
NAD+ + [glucose-6-phosphate dehydrogenase]-N6-acetyl-L-lysine
nicotinamide + [glucose-6-phosphate dehydrogenase]-L-lysine + 2'-O-acetyl-ADP-ribose
-
-
-
-
?
NAD+ + [isocitrate dehydrogenase 2]-N6-acetyl-L-lysine
nicotinamide + [isocitrate dehydrogenase 2]-L-lysine + 2'-O-acetyl-ADP-ribose
-
-
-
-
?
NAD+ + [N-hydroxyarylamine O-acetyltransferase]-N6-acetyl-L-lysine
nicotinamide + [N-hydroxyarylamine O-acetyltransferase]-L-lysine + 2'-O-acetyl-ADP-ribose
NAD+ + [protein]-N6-acetyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-acetyl-ADP-ribose
NAD+ + [protein]-N6-malonyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-malonyl-ADP-ribose
NAD+ + [protein]-N6-succinyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-succinyl-ADP-ribose
NAD+ + [PrpE protein]-N6-propionyl-L-lysine
nicotinamide + [PrpE protein]-L-lysine + 2'-O-propionyl-ADP-ribose
-
N-Lysine propionylation controls the activity of propionyl-CoA synthetase
-
-
?
NAD+ + [pyruvate dehydrogenase complex]-N6-succinyl-L-lysine
nicotinamide + [pyruvate dehydrogenase complex]-L-lysine + O-succinyl-ADP-ribose
-
SIRT5 represses biochemical activity of, and cellular respiration through, the protein complex
-
-
?
NAD+ + [RcsB protein]-N6-acetyl-L-lysine180
nicotinamide + [RcsB protein]-L-lysine180 + 2'-O-acetyl-ADP-ribose
NAD+ + [response regulator CheY]-N6-acetyl-L-lysine
nicotinamide + [response regulator CheY]-L-lysine + 2'-O-acetyl-ADP-ribose
NAD+ + [succinate dehydrogenase]-N6-succinyl-L-lysine
nicotinamide + [succinate dehydrogenase]-L-lysine + O-succinyl-ADP-ribose
-
SIRT5 represses biochemical activity of, and cellular respiration through, the protein complex
-
-
?
NAD+ + [urate oxidase]-N6-acetyl-L-lysine
nicotinamide + [urate oxidase]-L-lysine + 2'-O-acetyl-ADP-ribose
-
SIRT5 activates urate oxidase through deacetylation in mouse liver mitochondria
-
-
?
additional information
?
-
-
it is proposed that YfiQ and CobB catalyze the reversible acetylation of a protein that mediates carbon-induced cpxP transcription
-
-
-
NAD+ + [N-hydroxyarylamine O-acetyltransferase]-N6-acetyl-L-lysine
nicotinamide + [N-hydroxyarylamine O-acetyltransferase]-L-lysine + 2'-O-acetyl-ADP-ribose
-
-
-
-
?
NAD+ + [N-hydroxyarylamine O-acetyltransferase]-N6-acetyl-L-lysine
nicotinamide + [N-hydroxyarylamine O-acetyltransferase]-L-lysine + 2'-O-acetyl-ADP-ribose
-
-
-
-
?
NAD+ + [protein]-N6-acetyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-acetyl-ADP-ribose
-
the enzyme regulates protein function in diverse and often essential cellular processes, most notably translation
-
-
?
NAD+ + [protein]-N6-acetyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-acetyl-ADP-ribose
-
weak deacetylase activity
-
-
?
NAD+ + [protein]-N6-malonyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-malonyl-ADP-ribose
-
-
-
-
?
NAD+ + [protein]-N6-malonyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-malonyl-ADP-ribose
-
-
-
-
?
NAD+ + [protein]-N6-succinyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-succinyl-ADP-ribose
-
-
-
-
?
NAD+ + [protein]-N6-succinyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-succinyl-ADP-ribose
-
protein lysine succinylation may represent a posttranslational modification that can be reversed by Sirt5 in vivo. Lysine succinylation occurs on several mammalian proteins
-
-
?
NAD+ + [protein]-N6-succinyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-succinyl-ADP-ribose
-
strong succinylase activity
-
-
?
NAD+ + [protein]-N6-succinyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-succinyl-ADP-ribose
-
-
-
-
?
NAD+ + [RcsB protein]-N6-acetyl-L-lysine180
nicotinamide + [RcsB protein]-L-lysine180 + 2'-O-acetyl-ADP-ribose
-
acetylation of the response regulator RcsB controls transcription from the small RNA promoter rprA
-
-
?
NAD+ + [RcsB protein]-N6-acetyl-L-lysine180
nicotinamide + [RcsB protein]-L-lysine180 + 2'-O-acetyl-ADP-ribose
-
reversible Nepsilon-Lys acetylation of transcription factors is a mode of regulation of gene expression used by all cells
-
-
?
NAD+ + [response regulator CheY]-N6-acetyl-L-lysine
nicotinamide + [response regulator CheY]-L-lysine + 2'-O-acetyl-ADP-ribose
-
the enzyme regulates chemotaxis of Escherichia coli by deacetylating CheY
-
-
?
NAD+ + [response regulator CheY]-N6-acetyl-L-lysine
nicotinamide + [response regulator CheY]-L-lysine + 2'-O-acetyl-ADP-ribose
Escherichia coli W3110 / ATCC 27325
-
the enzyme regulates chemotaxis of Escherichia coli by deacetylating CheY
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
-
the zinc-binding domain of the sirtuin proteins may play a similar role in substrate-specific recognition
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(5E)-1-ethyl-5-(1H-indol-3-ylmethylidene)-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
-
-
(5E)-5-(1H-indol-3-ylmethylidene)-1-methyl-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
-
-
(5E)-5-[4-(benzyloxy)benzylidene]-1-(prop-2-en-1-yl)-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
-
-
(5E)-5-[4-(benzyloxy)benzylidene]-1-ethyl-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
-
-
(5E)-5-[4-(benzyloxy)benzylidene]-1-methyl-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
-
-
(5E)-5-[[5-(2,3-dichlorophenyl)furan-2-yl]methylidene]-1-(prop-2-en-1-yl)-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
-
-
3-(3,5-dibromo-4-hydroxybenzyliden)-5-iodo-1,3-dihydroindol-2-one
-
i.e. GW5074, potent inhibitor for desuccinylation activity of Sirt5. 0.1 mM inhibitor reduces Sirt5 desuccinylation activity (substrate: SKEYFS-(succinylLys)-QK) to about 15%. Weaker effects in Sirt5 deacetylation assays. Deacetylation activity is reduced to about 30% in presence of 0.1 mM inhibitor
5-[(1-benzyl-1H-indol-3-yl)methylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
-
-
5-[(6-methoxynaphthalen-1-yl)methylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
-
-
5-[4-[(2-chlorobenzyl)oxy]-3-methoxybenzylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
-
-
5-[4-[(4-bromobenzyl)oxy]benzylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
-
-
5-[[5-(2,3-dichlorophenyl)furan-2-yl]methylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
-
-
nicotinamide
-
nicotinamide inhibition of Sirt5-dependent deacetylation features weak substrate-dependence but requires high, nonphysiological nicotinamide concentrations. The insensitivity of Sirt5 to physiological nicotinamide concentrations is due to a lack of non-competitive inhibition via base exchange, and the inhibition observed at very high nicotinamide concentrations is likely caused by competition with NAD+
suramin
-
suramin binds into the NAD+-, the product-, and the substrate-binding site
additional information
-
not inhibited by EX527 (i.e. 6-chloro-2,3,4,9-tetrahydro-1H-carbazole-1-carboxamide)
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
resveratrol
-
0.2 mM resveratrol can stimulate the Sirt5 deacetylase activity against the fluorophore-modified peptide substrate Fluor-de-Lys
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.086
[histone H3 K9 peptide]-N6-succinyl-L-lysine
-
pH 8.0, 37°C, wild-type enzyme
-
0.069
NAD+
-
wild type enzyme, with [protein]-N6-succinyl-L-lysine as cosubstrate, at 8.0 pH and 25°C
0.15
NAD+
-
cosubstrate: Ac-(N6-succinyl)Lys-7-amido-4-methylcoumarin, pH 8.0, 37°C
0.321
NAD+
-
mutant enzyme Y102A, with [protein]-N6-succinyl-L-lysine as cosubstrate, at 8.0 pH and 25°C
0.609
NAD+
-
mutant enzyme R105I, with [protein]-N6-acetyl-L-lysine as cosubstrate, at 8.0 pH and 25°C
1.194
NAD+
-
mutant enzyme Y102A/R105I, with [protein]-N6-acetyl-L-lysine as cosubstrate, at 8.0 pH and 25°C
1.605
NAD+
-
mutant enzyme Y102A, with [protein]-N6-acetyl-L-lysine as cosubstrate, at 8.0 pH and 25°C
0.0147
[histone H3 K9 peptide]-N6-acetyl-L-lysine
-
pH 8.0, 37°C, mutant enzyme Y92F
-
0.0151
[histone H3 K9 peptide]-N6-acetyl-L-lysine
-
pH 8.0, 37°C, wild-type enzyme
-
0.02
[histone H3 K9 peptide]-N6-acetyl-L-lysine
-
pH 8.0, 37°C, mutant enzyme R95M
-
0.388
[protein]-N6-succinyl-L-lysine
-
mutant enzyme Y102A/R105I, at 8.0 pH and 25°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.242
[histone H3 K9 peptide]-N6-succinyl-L-lysine
-
pH 8.0, 37°C, wild-type enzyme
-
0.000026
NAD+
-
mutant enzyme Y102A/R105I, with [protein]-N6-acetyl-L-lysine as cosubstrate, at 8.0 pH and 25°C
0.000122
NAD+
-
mutant enzyme R105I, with [protein]-N6-acetyl-L-lysine as cosubstrate, at 8.0 pH and 25°C
0.000274
NAD+
-
mutant enzyme Y102A, with [protein]-N6-succinyl-L-lysine as cosubstrate, at 8.0 pH and 25°C
0.04
NAD+
-
wild type enzyme, with [protein]-N6-succinyl-L-lysine as cosubstrate, at 8.0 pH and 25°C
0.052
[histone H3 K9 peptide]-N6-acetyl-L-lysine
-
pH 8.0, 37°C, mutant enzyme Y92F
-
0.059
[histone H3 K9 peptide]-N6-acetyl-L-lysine
-
pH 8.0, 37°C, mutant enzyme R95M
-
0.135
[histone H3 K9 peptide]-N6-acetyl-L-lysine
-
pH 8.0, 37°C, wild-type enzyme
-
0.000026
[protein]-N6-succinyl-L-lysine
-
mutant enzyme Y102A/R105I, at 8.0 pH and 25°C
0.000274
[protein]-N6-succinyl-L-lysine
-
mutant enzyme R105I, at 8.0 pH and 25°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3
[histone H3 K9 peptide]-N6-acetyl-L-lysine
-
pH 8.0, 37°C, mutant enzyme R95M
-
3.5
[histone H3 K9 peptide]-N6-acetyl-L-lysine
-
pH 8.0, 37°C, mutant enzyme Y92F
-
8.9
[histone H3 K9 peptide]-N6-acetyl-L-lysine
-
pH 8.0, 37°C, wild-type enzyme
-
0.022
[histone H3 K9 peptide]-N6-succinyl-L-lysine
-
pH 8.0, 37°C, mutant enzyme R95M
-
0.067
[histone H3 K9 peptide]-N6-succinyl-L-lysine
-
pH 8.0, 37°C, mutant enzyme Y92F
-
2.8
[histone H3 K9 peptide]-N6-succinyl-L-lysine
-
pH 8.0, 37°C, wild-type enzyme
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0381
benzoyl-GVL(N6-(N-benzyloxycarbonyl-L-aspartyl))KEYGV-amide
-
pH 7.8, 37°C
0.0249
benzoyl-GVL(N6-(N-phthaloyl-DL-gamma-glutamyl))KEYGV-amide
-
pH 7.8, 37°C
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0559
(5E)-1-ethyl-5-(1H-indol-3-ylmethylidene)-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
-
pH 8.0, 37°C
0.027
(5E)-5-(1H-indol-3-ylmethylidene)-1-methyl-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
-
pH 8.0, 37°C
0.0673
(5E)-5-[4-(benzyloxy)benzylidene]-1-(prop-2-en-1-yl)-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
-
pH 8.0, 37°C
0.0129
(5E)-5-[4-(benzyloxy)benzylidene]-1-ethyl-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
-
pH 8.0, 37°C
0.0178
(5E)-5-[4-(benzyloxy)benzylidene]-1-methyl-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
-
pH 8.0, 37°C
0.0023
(5E)-5-[[5-(2,3-dichlorophenyl)furan-2-yl]methylidene]-1-(prop-2-en-1-yl)-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
-
pH 8.0, 37°C
0.001
(N6-thiosuccinyl)KSTGGKA
Homo sapiens
-
pH and temperature not specified in the publication
0.0465
5-(1H-indol-3-ylmethylidene)-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
-
pH 8.0, 37°C
0.03
5-(biphenyl-4-ylmethylidene)-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
-
pH 8.0, 37°C
0.0166
5-[(1-benzyl-1H-indol-3-yl)methylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
-
pH 8.0, 37°C
0.0224
5-[(6-methoxynaphthalen-1-yl)methylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
-
pH 8.0, 37°C
0.0126
5-[4-(benzyloxy)benzylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
-
pH 8.0, 37°C
0.0394
5-[4-(propan-2-yl)benzylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
-
pH 8.0, 37°C
0.0124
5-[4-[(2-chlorobenzyl)oxy]-3-methoxybenzylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
-
pH 8.0, 37°C
0.0062
5-[4-[(4-bromobenzyl)oxy]benzylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
-
pH 8.0, 37°C
0.0036
5-[[5-(2,3-dichlorophenyl)furan-2-yl]methylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
-
pH 8.0, 37°C
0.04
Ac-AR(N6-thiosuccinyl)KST-NH2
Homo sapiens
-
pH and temperature not specified in the publication
0.025
Ac-RR(N6-thiosuccinyl)KRR-NH2
Homo sapiens
-
pH and temperature not specified in the publication
0.03
AR(N6-thiosuccinyl)KST
Homo sapiens
-
pH and temperature not specified in the publication
0.001
KQTAR(N6-thiosuccinyl)K
Homo sapiens
-
pH and temperature not specified in the publication
0.005
KQTAR(N6-thiosuccinyl)KSTGGKA
Homo sapiens
-
pH and temperature not specified in the publication
0.0195
3-(3,5-dibromo-4-hydroxybenzyliden)-5-iodo-1,3-dihydroindol-2-one
Homo sapiens
-
pH 7.5, temperature not specified in the publication, substrate: SKEYFS-(succinylLys)-QK
0.097
3-(3,5-dibromo-4-hydroxybenzyliden)-5-iodo-1,3-dihydroindol-2-one
Homo sapiens
-
pH 7.5, temperature not specified in the publication, substrate: FKRGVL-(acetylLys)-EYGVKV
0.0111
Isonicotinamide
Homo sapiens
-
wild type enzyme, with 0.05 mM NAD+, at 8.0 pH and 25°C
0.0142
suramin
Homo sapiens
-
pH 7.5, temperature not specified in the publication, substrate: acetylated peptide derived from carbamoylphosphate synthetase 1 (CPS1)
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Escherichia coli W3110 / ATCC 27325
strain W3110 is a K12 derivative that is wild-type for chemotaxis
-
-
brenda
strain W3110 is a K12 derivative that is wild-type for chemotaxis
-
-
brenda
-
728857, 728962, 729138, 729372, 729547, 729801, 729885, 729993, 730024, 730161, 730205, 730245, 730474, 730706, 730713, 730922, 730964, 730974, 731010, 738843, 739445
SwissProt
brenda
-
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
in the cerebellar cortex, SIRT5 can be found in Purkinje cells, and is mainly distributed in the cytoplasm, but is not markedly expressed in the molecular layer or granular layer cells
brenda
-
SIRT5 is overexpressed in human non-small cell lung cancer cells, high expression of SIRT5 predicts poor survival
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
SIRT5 isoforms (i.e., SIRT5iso1 and SIRT5iso2) are encoded by the human SIRT5 gene. Their C-termini slightly differ from each other. Although both isoforms contain cleavable mitochondrial targeting signals at their N-termini,it is found that the cleaved SIRT5iso2 is localized mainly in mitochondria, whereas the cleaved SIRT5iso1 is localized in both mitochondria and cytoplasm. The cytoplasmic localization of cleaved SIRT5iso1 is dependent on the SIRT5iso1-specific C-terminus
brenda
-
mainly distributed in the cytoplasm of Purkinje cells
brenda
-
SIRT5 isoforms (i.e., SIRT5iso1 and SIRT5iso2) are encoded by the human SIRT5 gene. Their C-termini slightly differ from each other. Although both isoforms contain cleavable mitochondrial targeting signals at their N-termini, it is found that the cleaved SIRT5iso2 is localized mainly in mitochondria, whereas the cleaved SIRT5iso1 is localized in both mitochondria and cytoplasm. The C-terminus of SIRT5iso2, which is rich in hydrophobic amino acid residues, functions as a mitochondrial membrane insertion signal
brenda
-
Sirt5 can be translocated into the mitochondrial intermembrane space, but also into the matrix
brenda
-
SIRT5 is present both mitochondrially and extramitochondrially
brenda
-
a very small amount of SIRT5 is detected in the nuclear fraction
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
-
acetyl-coenzyme A synthetase overproduced by the cobB deletion mutant strain contains acetyllysine at residue Lys609
malfunction
-
SIRT5 knockdown in cardiomyocytes results in a marked reduction in cell viability, and a significant increase in the number of apoptotic cells
malfunction
-
RcsB protein isolated from a cobB deletion mutation strain is hyperacetylated
malfunction
-
CobB knockout cells show slightly increased acetylation levels and succinylation levels relative to the wild type cells
malfunction
-
deletion of Sirt5 in mice increases the level of succinylation on carbamoyl phosphate synthase 1
malfunction
-
SIRT5 knockdown represses lung cancer cell growth and transformation in vitro and in vivo. SIRT5 knockdown makes lung cancer cells more sensitive to drug (cis-diamminedichloroplatinum, 5-fluorouracil or bleomycin) treatment in vitro and in vivo. Nrf2, which is a core transcription factor for lung cancer growth and drug resistance, is a target of SIRT5
malfunction
-
knockdown or knockout of the enzyme leads to high levels of cellular reactive oxygen species. SIRT5 inactivation leads to the inhibition of isocitrate dehydrogenase 2 and glucose-6-phosphate dehydrogenase, thereby decreasing NADPH production, lowering GSH, impairing the ability to scavenge ROS, and increasing cellular susceptibility to oxidative stress
metabolism
-
because ammonia generated during fasting is toxic, SIRT5 might play a protective role by converting ammonia to non-toxic urea through deacetylation and activation of carbamoyl phosphate synthase 1
metabolism
-
SIRT5 plays a pivotal role in ammonia detoxification and disposal by activating carbamoyl phosphate synthetase 1 an enzyme, catalyzing the initial step of the urea cycle for ammonia detoxification and disposal
metabolism
-
SIRT5 deacetylates carbamoyl phosphate synthetase 1 (CPS1), an enzyme which is the first and rate-limiting step of urea cycle. Deacetylation of CPS1 by SIRT5 results in activation of CPS1 enzymatic activity; SIRT5 has an emerging role in the metabolic adaptation to fasting, high protein diet and calorie restriction
metabolism
-
SIRT5 is involved in the regulation of oxidative stress induced apoptosis in cardiomyocytes
metabolism
-
the enzyme is involved in regulation of mitochondrial energy metabolism
metabolism
-
human SIRT5 potentially controls various primate-specific functions via two isoforms with different intracellular localizations or stabilities
metabolism
-
sirtuin deacetylase CobB deficiency leads to both site-specific and global changes in protein acetylation stoichiometry, affecting central metabolism
metabolism
-
overexpression of CobB reduces the 6fold glucose-dependent induction to a more modest 3fold induction; the Gcn5-like acetyltransferase YfiQ and the sirtuin deacetylase CobB play crucial roles in the transcription regulation of the periplasmic stress-responsive promoter cpxP when cells of Escherichia coli grow in the presence of glucose, an environment that induces protein acetylation
metabolism
-
reversible Nepsilon-Lys acetylation of transcription factors is a mode of regulation of gene expression used by all cells
metabolism
-
SIRT5 is a protein responsible for growth and drug resistance in human non-small cell lung cancer cells
physiological function
-
deacetylation by CobB activates the acetyl-coenzyme A synthetase
physiological function
-
SIRT5 overexpression increases ATP synthesis and oxygen consumption in HepG2 cells, but does not affect mitochondrial biogenesis
physiological function
-
acetylation of the response regulator RcsB controls transcription from the small RNA promoter rprA
physiological function
-
the enzyme regulates protein function in diverse and often essential cellular processes, most notably translation. CobB is the predominate deacetylase in Escherichia coli loop or a helix that protrudes into the solution and thus in position to be an easily accessible target
physiological function
-
SIRT5 is a central regulator of Lys succinylation in mammalian cells
physiological function
-
the enzyme regulates chemotaxis of Escherichia coli by deacetylating CheY
physiological function
-
SIRT5 is involved in influencing oocyte quality and in-vitro-fertilisation outcomes
physiological function
-
protein lysine succinylation may represent a posttranslational modification that can be reversed by Sirt5
physiological function
-
the enzyme prevents cigarette smoke extract-induced apoptosis in lung epithelial cells via deacetylation of FOXO3
physiological function
Escherichia coli W3110 / ATCC 27325
-
the enzyme regulates chemotaxis of Escherichia coli by deacetylating CheY
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
NPD1_ARCFU
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
245
0
27143
Swiss-Prot
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CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method at 4°C, crystal structure of wild-type enzyme, mutant enzyme S24A, mutant enzyme H80N, mutant enzyme F159A, and triple Sir2 mutant (D102G/F159A/R170A)
-
vapor diffusion at 20°C, crystal structure of the enzyme bound to KGLGKGGA(N6-succinyl)KRHRKW
-
crystals of native and selenomethionine-derivatized cobB are grown at room temperature using the hanging-drop, vapor-diffusion method. The crystal structure of the Escherichia coli cobB core domain (residues 40–274) in complex with an 11-residue peptide containing residues 12–19 of histone H4 and acetylated at lysine 16 is determined by a combination of Zn2+ and Se multiwavelength anomalous diffraction to 1.96 A resolution
-
crystal structure of Sirt5 in complex with a thioacetyl peptide is obtained, The corresponding acetyl peptide could not be crystallized with Sirt5
-
crystal structure of Sirt5 in complex with fluor-de-Lys peptide and resveratrol and crystal structure of Sirt5 in complex with fluor-de-Lys peptide and piceatannol
-
crystal structures of a binary complex of SIRT5 with an H3K9 succinyl peptide and a binary complex of SIRT5 with a bicyclic intermediate obtained by incubating SIRT5-H3K9 thiosuccinyl peptide co-crystals with NAD+
-
hanging drop vapor diffusion method at 18°C. X-ray crystal structures of the ternary complex of SIRT5 bound to a peptide substrate and carba-NAD+ (an unreactive NAD+ analogue)
-
hanging drop vapor-diffusion method at 20°C. Crystal structures of SIRT5 in complex with ADP-ribose, and crystal structures of SIRT5 bound to suramin
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D101N
-
the decreased NAD-dependent deacetylase activity for the mutant proteins is at least partly due to reduced binding affinities for NAD+
F159A
-
the Km value of the mutant enzyme is twice that of wild type enzyme, whereas the kcat is 5fold less. In the F159A mutant, two water molecules occupy the position of the Phe159 ring
H80N
-
mutant retains about 60% of the NAD binding ability of wild type Sir2
S24A
-
the decreased NAD-dependent deacetylase activity for the mutant proteins is at least partly due to reduced binding affinities for NAD+
R95M
-
desuccinylation decreases about 100fold, deacetylation decreases about 3fold
Y92F
-
desuccinylation decreases about 42fold, deacetylation decreases about 3fold
R105L
Y102A
-
the mutant enzyme catalyzes both deacetylation and desuccinylation reactions with comparable efficiencies
Y102A/R105I
-
the mutant enzyme favores the deacetylase reaction over the desuccinylation reaction
R105L
-
mutant retains wild-type deacetylation activity and partially gains Sirt3-like nicotinamide sensitivity (IC50: 0.189 mM)
R105L
-
the mutant enzyme favores the deacetylase reaction over the desuccinylation reaction
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
a de novo protein synthesis inhibition experiment using cycloheximide shows that the SIRT5iso1-specific C-terminus is necessary for maintaining the stability of SIRT5iso1
-
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PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
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CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
crystals are grown by hanging drop vapor diffusion method, truncated SIRT5(34–302) is cloned and expressed in Escherichia coli
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enhanced expression of SIRT5 in the cerebral tissue of calorie restriction rats compared with rats that remained fed ad libitum
-
overexpression of AMP-activated protein kinase (AMPK) in mouse hepatocytes downregulates expression of SIRT5 mRNA by 58%. The antidiabetes drug metformin (1 mM), an established AMPK activator, reduces the mouse SIRT5 protein level by 44% in cultured hepatocytes and by 31% in liver in vivo (300 mg/kg, 7 d)
-
SIRT5 is significantly down-regulated in cardiomyocytes upon oxidative stress
-
women with reduced ovarian reserve or advanced maternal age have decreased SIRT5 mRNA, protein and desuccinylation activity in granulosa and cumulus cells
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
pharmacological interventions on SIRT5 expression may be useful in the treatment of oxidative stress-related cardiac injury
medicine
-
SIRT5 is involved in influencing oocyte quality and in-vitro-fertilisation outcomes
medicine
-
SIRT5 may serve as a potential prognostic factor and drug target for intervention in non-small cell lung cancer. SIRT5 is overexpressed in human non-small cell lung cancer cells, high expression of SIRT5 predicts poor survival. SIRT5 knockdown makes lung cancer cells more sensitive to drug (cis-diamminedichloroplatinum, 5-fluorouracil or bleomycin) treatment in vitro and in vivo. Nrf2, which is a core transcription factor for lung cancer growth and drug resistance, is a target of SIRT5
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Starai, V.J.; Celic, I.; Cole, R.N.; Boeke, J.D.; Escalante-Semerena, J.C.
Sir2-dependent activation of acetyl-CoA synthetase by deacetylation of active lysine
Science
298
2390-2392
2002
Salmonella enterica
brenda
Ogura, M.; Nakamura, Y.; Tanaka, D.; Zhuang, X.; Fujita, Y.; Obara, A.; Hamasaki, A.; Hosokawa, M.; Inagaki, N.
Overexpression of SIRT5 confirms its involvement in deacetylation and activation of carbamoyl phosphate synthetase 1
Biochem. Biophys. Res. Commun.
393
73-78
2010
Mus musculus (Q8K2C6)
brenda
Nakagawa, T.; Lomb, D.J.; Haigis, M.C.; Guarente, L.
SIRT5 deacetylates carbamoyl phosphate synthetase 1 and regulates the urea cycle
Cell
137
560-570
2009
Mus musculus (Q8K2C6)
brenda
Maurer, B.; Rumpf, T.; Scharfe, M.; Stolfa, D.A.; Schmitt, M.L.; He, W.; Verdin, E.; Sippl, W.; Jung, M.
Inhibitors of the NAD(+)-dependent protein desuccinylase and demalonylase Sirt5
ACS Med. Chem. Lett.
3
1050-1053
2012
Homo sapiens (Q9NXA8)
brenda
Nakagawa, T.; Guarente, L.
Urea cycle regulation by mitochondrial sirtuin, SIRT5
Aging
1
578-581
2009
Mus musculus (Q8K2C6)
brenda
Roessler, C.; Nowak, T.; Pannek, M.; Gertz, M.; Nguyen, G.T.; Scharfe, M.; Born, I.; Sippl, W.; Steegborn, C.; Schutkowski, M.
Chemical probing of the human sirtuin 5 active site reveals its substrate acyl specificity and peptide-based inhibitors
Angew. Chem. Int. Ed. Engl.
53
10728-10732
2014
Homo sapiens, Homo sapiens (Q9NXA8)
brenda
Lin, Z.F.; Xu, H.B.; Wang, J.Y.; Lin, Q.; Ruan, Z.; Liu, F.B.; Jin, W.; Huang, H.H.; Chen, X.
SIRT5 desuccinylates and activates SOD1 to eliminate ROS
Biochem. Biophys. Res. Commun.
441
191-195
2013
Homo sapiens, Homo sapiens (Q9NXA8)
brenda
Suenkel, B.; Fischer, F.; Steegborn, C.
Inhibition of the human deacylase Sirtuin 5 by the indole GW5074
Bioorg. Med. Chem. Lett.
23
143-146
2012
Homo sapiens, Homo sapiens (Q9NXA8)
brenda
Tan, M.; Peng, C.; Anderson, K.A.; Chhoy, P.; Xie, Z.; Dai, L.; Park, J.; Chen, Y.; Huang, H.; Zhang, Y.; Ro, J.; Wagner, G.R.; Green, M.F.; Madsen, A.S.; Schmiesing, J.; Peterson, B.S.; Xu, G.; Ilkayeva, O.R.; Muehlbauer, M.J.; Braulke, T.; Mühlhausen, C.; Backos, D.S.; Olsen, C.A.; McGuire, P.J.; Pletcher, S.D.; Lombard, D.B.; Hirschey, M.D.; Zhao, Y.
Lysine glutarylation is a protein posttranslational modification regulated by SIRT5
Cell Metab.
19
605-617
2014
Homo sapiens (Q9NXA8)
brenda
Liu, B.; Che, W.; Zheng, C.; Liu, W.; Wen, J.; Fu, H.; Tang, K.; Zhang, J.; Xu, Y.
SIRT5: a safeguard against oxidative stress-induced apoptosis in cardiomyocytes
Cell. Physiol. Biochem.
32
1050-1059
2013
Rattus norvegicus (Q68FX9)
brenda
Buler, M.; Aatsinki, S.M.; Izzi, V.; Uusimaa, J.; Hakkola, J.
SIRT5 is under the control of PGC-1alpha and AMPK and is involved in regulation of mitochondrial energy metabolism
FASEB J.
28
3225-3237
2014
Mus musculus, Mus musculus (Q8K2C6)
brenda
Zhang, Q.F.; Gu, J.; Gong, P.; Wang, X.D.; Tu, S.; Bi, L.J.; Yu, Z.N.; Zhang, Z.P.; Cui, Z.Q.; Wei, H.P.; Tao, S.C.; Zhang, X.E.; Deng, J.Y.
Reversibly acetylated lysine residues play important roles in the enzymatic activity of Escherichia coli N-hydroxyarylamine O-acetyltransferase
FEBS J.
280
1966-1979
2013
Escherichia coli, Escherichia coli AD494
brenda
Nakamura, Y.; Ogura, M.; Ogura, K.; Tanaka, D.; Inagaki, N.
SIRT5 deacetylates and activates urate oxidase in liver mitochondria of mice
FEBS Lett.
586
4076-4081
2012
Mus musculus, Mus musculus (Q8K2C6)
brenda
Matsushita, N.; Yonashiro, R.; Ogata, Y.; Sugiura, A.; Nagashima, S.; Fukuda, T.; Inatome, R.; Yanagi, S.
Distinct regulation of mitochondrial localization and stability of two human Sirt5 isoforms
Genes Cells
16
190-202
2011
Homo sapiens, Homo sapiens (Q9NXA8)
brenda
He, B.; Du, J.; Lin, H.
Thiosuccinyl peptides as Sirt5-specific inhibitors
J. Am. Chem. Soc.
134
1922-1925
2012
Homo sapiens, Homo sapiens (Q9NXA8)
brenda
Hu, L.I.; Chi, B.K.; Kuhn, M.L.; Filippova, E.V.; Walker-Peddakotla, A.J.; Bäsell, K.; Becher, D.; Anderson, W.F.; Antelmann, H.; Wolfe, A.J.
Acetylation of the response regulator RcsB controls transcription from a small RNA promoter
J. Bacteriol.
195
4174-4186
2013
Escherichia coli
brenda
Chang, J.H.; Kim, H.C.; Hwang, K.Y.; Lee, J.W.; Jackson, S.P.; Bell, S.D.; Cho, Y.
Structural basis for the NAD-dependent deacetylase mechanism of Sir2
J. Biol. Chem.
277
34489-34498
2002
Archaeoglobus fulgidus (O28597)
brenda
Garrity, J.; Gardner, J.G.; Hawse, W.; Wolberger, C.; Escalante-Semerena, J.C.
N-Lysine propionylation controls the activity of propionyl-CoA synthetase
J. Biol. Chem.
282
30239-30245
2007
Salmonella enterica
brenda
Zhou, Y.; Zhang, H.; He, B.; Du, J.; Lin, H.; Cerione, R.A.; Hao, Q.
The bicyclic intermediate structure provides insights into the desuccinylation mechanism of human sirtuin 5 (SIRT5)
J. Biol. Chem.
287
28307-28314
2012
Homo sapiens, Homo sapiens (Q9NXA8)
brenda
Feldman, J.L.; Baeza, J.; Denu, J.M.
Activation of the protein deacetylase SIRT6 by long-chain fatty acids and widespread deacylation by mammalian sirtuins
J. Biol. Chem.
288
31350-31356
2013
Homo sapiens (Q9NXA8)
brenda
Baeza, J.; Dowell, J.A.; Smallegan, M.J.; Fan, J.; Amador-Noguez, D.; Khan, Z.; Denu, J.M.
Stoichiometry of site-specific lysine acetylation in an entire proteome
J. Biol. Chem.
289
21326-21338
2014
Escherichia coli
brenda
Geng, Y.Q.; Li, T.T.; Liu, X.Y.; Li, Z.H.; Fu, Y.C.
SIRT1 and SIRT5 activity expression and behavioral responses to calorie restriction
J. Cell. Biochem.
112
3755-3761
2011
Rattus norvegicus (Q68FX9)
brenda
Madsen, A.S.; Olsen, C.A.
Substrates for efficient fluorometric screening employing the NAD-dependent sirtuin 5 lysine deacylase (KDAC) enzyme
J. Med. Chem.
55
5582-5590
2012
Homo sapiens, Homo sapiens (Q9NXA8)
brenda
Zhao, K.; Chai, X.; Marmorstein, R.
Structure and substrate binding properties of cobB, a Sir2 homolog protein deacetylase from Escherichia coli
J. Mol. Biol.
337
731-741
2004
Escherichia coli, Escherichia coli (P75960)
brenda
Schlicker, C.; Gertz, M.; Papatheodorou, P.; Kachholz, B.; Becker, C.F.; Steegborn, C.
Substrates and regulation mechanisms for the human mitochondrial sirtuins Sirt3 and Sirt5
J. Mol. Biol.
382
790-801
2008
Homo sapiens, Homo sapiens (Q9NXA8)
brenda
Szczepankiewicz, B.G.; Dai, H.; Koppetsch, K.J.; Qian, D.; Jiang, F.; Mao, C.; Perni, R.B.
Synthesis of carba-NAD and the structures of its ternary complexes with SIRT3 and SIRT5
J. Org. Chem.
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2012
Homo sapiens, Homo sapiens (Q9NXA8)
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AbouElfetouh, A.; Kuhn, M.L.; Hu, L.I.; Scholle, M.D.; Sorensen, D.J.; Sahu, A.K.; Becher, D.; Antelmann, H.; Mrksich, M.; Anderson, W.F.; Gibson, B.W.; Schilling, B.; Wolfe, A.J.
The E. coli sirtuin CobB shows no preference for enzymatic and nonenzymatic lysine acetylation substrate sites
Microbiologyopen
4
66-83
2015
Escherichia coli (P75960)
brenda
Peng, C.; Lu, Z.; Xie, Z.; Cheng, Z.; Chen, Y.; Tan, M.; Luo, H.; Zhang, Y.; He, W.; Yang, K.; Zwaans, B.M.; Tishkoff, D.; Ho, L.; Lombard, D.; He, T.C.; Dai, J.; Verdin, E.; Ye, Y.; Zhao, Y.
The first identification of lysine malonylation substrates and its regulatory enzyme
Mol. Cell. Proteomics
10
0000
2011
Mus musculus (Q8K2C6)
brenda
Colak, G.; Xie, Z.; Zhu, A.Y.; Dai, L.; Lu, Z.; Zhang, Y.; Wan, X.; Chen, Y.; Cha, Y.H.; Lin, H.; Zhao, Y.; Tan, M.
Identification of lysine succinylation substrates and the succinylation regulatory enzyme CobB in Escherichia coli
Mol. Cell. Proteomics
12
3509-3520
2013
Escherichia coli
brenda
Park, J.; Chen, Y.; Tishkoff, D.X.; Peng, C.; Tan, M.; Dai, L.; Xie, Z.; Zhang, Y.; Zwaans, B.M.; Skinner, M.E.; Lombard, D.B.; Zhao, Y.
SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways
Mol. Cell.
50
919-930
2013
Mus musculus (Q8K2C6)
brenda
Li, R.; Gu, J.; Chen, Y.Y.; Xiao, C.L.; Wang, L.W.; Zhang, Z.P.; Bi, L.J.; Wei, H.P.; Wang, X.D.; Deng, J.Y.; Zhang, X.E.
CobB regulates Escherichia coli chemotaxis by deacetylating the response regulator CheY
Mol. Microbiol.
76
1162-1174
2010
Escherichia coli, Escherichia coli W3110 / ATCC 27325
brenda
Lima, B.P.; Antelmann, H.; Gronau, K.; Chi, B.K.; Becher, D.; Brinsmade, S.R.; Wolfe, A.J.
Involvement of protein acetylation in glucose-induced transcription of a stress-responsive promoter
Mol. Microbiol.
81
1190-1204
2011
Escherichia coli
brenda
Lutz, M.I.; Milenkovic, I.; Regelsberger, G.; Kovacs, G.G.
Distinct patterns of sirtuin expression during progression of Alzheimer's disease
Neuromolecular Med.
16
405-414
2014
Homo sapiens (Q9NXA8)
brenda
Thao, S.; Chen, C.S.; Zhu, H.; Escalante-Semerena, J.C.
Nepsilon-lysine acetylation of a bacterial transcription factor inhibits its DNA-binding activity
PLoS One
5
e15123
2010
Escherichia coli (P75960)
brenda
Fischer, F.; Gertz, M.; Suenkel, B.; Lakshminarasimhan, M.; Schutkowski, M.; Steegborn, C.
Sirt5 deacylation activities show differential sensitivities to nicotinamide inhibition
PLoS One
7
e45098
2012
Homo sapiens, Homo sapiens (Q9NXA8)
brenda
Gertz, M.; Nguyen, G.T.; Fischer, F.; Suenkel, B.; Schlicker, C.; Fränzel, B.; Tomaschewski, J.; Aladini, F.; Becker, C.; Wolters, D.; Steegborn, C.
A molecular mechanism for direct sirtuin activation by resveratrol
PLoS One
7
e49761
2012
Homo sapiens, Homo sapiens (Q9NXA8)
brenda
Ringel, A.E.; Roman, C.; Wolberger, C.
Alternate deacylating specificities of the archaeal sirtuins Sir2Af1 and Sir2Af2
Protein Sci.
23
1686-1697
2014
Archaeoglobus fulgidus, Archaeoglobus fulgidus (O28597), Escherichia coli
brenda
Pacella-Ince, L.; Zander-Fox, D.L.; Lane, M.
Mitochondrial SIRT5 is present in follicular cells and is altered by reduced ovarian reserve and advanced maternal age
Reprod. Fertil. Dev.
26
1072-1083
2014
Homo sapiens (Q9NXA8)
brenda
Du, J.; Zhou, Y.; Su, X.; Yu, J.J.; Khan, S.; Jiang, H.; Kim, J.; Woo, J.; Kim, J.H.; Choi, B.H.; He, B.; Chen, W.; Zhang, S.; Cerione, R.A.; Auwerx, J.; Hao, Q.; Lin, H.
Sirt5 is a NAD-dependent protein lysine demalonylase and desuccinylase
Science
334
806-809
2011
Homo sapiens (Q9NXA8), Mus musculus (Q8K2C6)
brenda
Schuetz, A.; Min, J.; Antoshenko, T.; Wang, C.L.; Allali-Hassani, A.; Dong, A.; Loppnau, P.; Vedadi, M.; Bochkarev, A.; Sternglanz, R.; Plotnikov, A.N.
Structural basis of inhibition of the human NAD+-dependent deacetylase SIRT5 by suramin
Structure
15
377-389
2007
Homo sapiens, Homo sapiens (Q9NXA8)
brenda
Lu, W.; Zuo, Y.; Feng, Y.; Zhang, M.
SIRT5 facilitates cancer cell growth and drug resistance in non-small cell lung cancer
Tumour Biol.
35
10699-10705
2014
Homo sapiens, Homo sapiens (Q9NXA8)
brenda
Wang, Y.; Zhu, Y.; Xing, S.; Ma, P.; Lin, D.
SIRT5 prevents cigarette smoke extract-induced apoptosis in lung epithelial cells via deacetylation of FOXO3
Cell Stress Chaperones
20
805-810
2015
Homo sapiens
brenda
Zhou, L.; Wang, F.; Sun, R.; Chen, X.; Zhang, M.; Xu, Q.; Wang, Y.; Wang, S.; Xiong, Y.; Guan, K.L.; Yang, P.; Yu, H.; Ye, D.
SIRT5 promotes IDH2 desuccinylation and G6PD deglutarylation to enhance cellular antioxidant defense
EMBO Rep.
17
811-822
2016
Mus musculus
brenda
Roessler, C.; Tueting, C.; Meleshin, M.; Steegborn, C.; Schutkowski, M.
A novel continuous assay for the deacylase sirtuin 5 and other deacetylases
J. Med. Chem.
58
7217-7223
2015
Homo sapiens (Q9NXA8)
brenda
Nishida, Y.; Rardin, M.J.; Carrico, C.; He, W.; Sahu, A.K.; Gut, P.; Najjar, R.; Fitch, M.; Hellerstein, M.; Gibson, B.W.; Verdin, E.
SIRT5 regulates both cytosolic and mitochondrial protein malonylation with glycolysis as a major target
Mol. Cell
59
321-332
2015
Mus musculus (Q8K2C6)
brenda
Yu, J.; Haldar, M.; Mallik, S.; Srivastava, D.K.
Role of the substrate specificity-defining residues of human SIRT5 in modulating the structural stability and inhibitory features of the enzyme
PLoS ONE
11
e0152467
2016
Homo sapiens, Homo sapiens (Q9NXA8)
brenda
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